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Information on EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase and Organism(s) Escherichia coli and UniProt Accession P50465
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4.2.99.18 DNA-(apurinic or apyrimidinic site) lyaseIUBMB Comments
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
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Word Map
- 4.2.99.18
- strand
-
exonuclease
- glycosylases
-
single-stranded
- pyrimidine
- endonucleases
- 8-oxoguanine
- nick
- thymine
- uracil
- duplex
-
genotoxic
- xrcc1
-
phosphodiester
- comet
- deoxyribose
- methanesulfonate
- mispairs
-
uracil-dna
-
depurinated
-
beta-elimination
-
excise
- formamidopyrimidine
-
3'-phosphatase
- 7,8-dihydro-8-oxoguanine
- tetrahydrofuran
-
site-containing
-
mutyh
-
endonucleolytic
-
xeroderma
- pigmentosum
-
base-excision
- 3'-phosphodiesterase
-
cross-complementing
- 8-oxo-7,8-dihydroguanine
- fen1
-
unrepaired
-
formamidopyrimidine-dna
-
incises
-
long-patch
-
dna-repair
-
uracil-containing
-
ser326cys
- dihydrouracil
-
arg399gln
- 3'-exonuclease
-
reduction-oxidation
-
enzyme-dna
- medicine
-
gap-filling
-
damage-specific
- analysis
- diagnostics
- biotechnology
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Synonyms
ap endonuclease, ref-1, ape1/ref-1, apex1, ape/ref-1, apurinic/apyrimidinic endonuclease 1, ap lyase, ape-1, alkbh1, endo iii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AP 1
-
-
-
-
AP Dnase
-
-
-
-
AP endo
-
-
-
-
AP endonuclease
AP endonuclease Class I
-
-
-
-
AP lyase
-
-
-
-
AP-endonuclease
-
-
-
-
Ape
-
-
-
-
APEN
-
-
-
-
APEX nuclease
-
-
-
-
APN1
-
-
-
-
apurinic DNA endonuclease
-
-
-
-
apurinic endodeoxyribonuclease
-
-
-
-
apurinic endonuclease
-
-
-
-
apurinic-apyrimidinic DNA endonuclease
-
-
-
-
apurinic-apyrimidinic endodeoxyribonuclease
-
-
-
-
apurinic-apyrimidinic endonuclease
-
-
-
-
apurinic/apyrimidinic lyase
-
-
-
-
apurinic/apyrimidinic specific endonuclease
-
-
-
-
apyrimidinic endonuclease
-
-
-
-
class II apurinic/apyrimidinic(AP)-endonuclease
-
-
-
-
deoxyribonuclease (apurinic or apyrimidinic)
-
-
-
-
E. coli endonuclease III
-
-
-
-
EcoNth
-
a bifunctional enzyme that has DNA glycosylase and apurinic/apyrimidinic lyase activity
Endo III
endodeoxyribonuclease
-
-
-
-
endodeoxyribonuclease III
-
-
-
-
endonuclease III
endonuclease IV
-
an abasic or apurinic-apyrimidinic endonuclease superfamily crucial for DNA base excision repair
endonuclease VI
-
-
-
-
Escherichia coli endonuclease III
-
-
-
-
HAP1
-
-
-
-
HAP1h
-
-
-
-
KsgA
-
a 16S rRNA adenine methyltransferase with DNA glycosylase/AP lyase activity
Micrococcus luteus UV endonuclease
-
-
-
-
MMH
-
-
-
-
Nfo
-
-
-
-
Ntg1p
-
-
-
-
Ntg2p
-
-
-
-
NTH1
-
-
-
-
nuclease, apurinic endodeoxyribo-
-
-
-
-
nuclease, apurinic-apyrimidinic endodeoxyribo-
-
-
-
-
nuclease, endodeoxyribo-, III
-
-
-
-
phage-T4 UV endonuclease
-
-
-
-
REF-1 protein
-
-
-
-
Ref1
-
-
-
-
UV endo V
-
-
-
-
UV endonuclease
-
-
-
-
UV endonuclease V
-
-
-
-
AP endonuclease
-
-
-
-
endonuclease III
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
CAS REGISTRY NUMBER
COMMENTARY
60184-90-9
-
61811-29-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
?
-
-
-
?
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
?
-
-
-
?
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
?
-
-
-
-
?
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
?
-
-
-
-
?
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
?
-
-
-
-
?
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
?
-
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
?
-
-
-
-
?
DNA
fragments of DNA
-
cleavage at abasic sites in duplexes with paired lesions is slower than in duplexes with single lesions. Double strand breaks are readily generated in duplexes with abasic sites positioned 3' to each other. In duplexes containing abasic sites set 1 base pair apart, 5' to each other, both enzymes slowly cleave the abasic site on one strand only and are unable to incise the other stand
-
?
DNA
fragments of DNA
-
removes 5-hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine via a N-glycosylase/beta-elimination reaction
-
?
DNA
fragments of DNA
-
cuts the DNA strands on the 5' side of the apurinic sites giving a 3'-OH and a 5'-phosphate
-
?
DNA
fragments of DNA
-
endonucleolytic cleavage near apurinic or apyrimidinic sites to products with 5'-phosphates, e.g. UV-irradiated poly(dA)*poly(dT)
-
?
DNA
fragments of DNA
-
catalyzes phosphodiester bond cleavage via a lyase- rather than a hydrolase mechanism
-
?
DNA
fragments of DNA
-
synthetic oligodeoxynucleotides containing abasic sites
-
?
DNA
fragments of DNA
-
endonuclease III: excision of a number of thymine- and cytosine-derived lesions from DNA, no purine-derived lesions excised by endonuclease III
-
?
DNA
fragments of DNA
-
endonucleolytic activity against apurinic and apyrimidinic sites and a dose-dependent response to DNA that has been X-irradiated, UV-irradiated or treated with OsO4
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
cleaves the phosphodiester bond 3' to the apurinic/apyrimidinic site
-
?
DNA
fragments of DNA
-
duplex oligonucleotides containing the base lesion analogs O-methylhydoxylamine or O-benzylhydroxylamine, N-glycosylase activity generates intermediary AP site which is subsequently cleaved by the enzyme -associated AP lyase activity, O-alkoxyamine-modified AP sites are poorer substrates than the presumed physiological substrates
-
?
DNA
fragments of DNA
-
enzyme generates only single-strand breaks when the base damage is set one and three base-pairs apart, and only slowly introduces double-strand breaks in substrates where base damage is set five or seven base-pairs apart. Treatment of an abasic site-containing DNA readily yields double-strand breaks.
-
?
DNA
fragments of DNA
-
DNA containing dihydrouridine, 5,3-dihydrothymidine, 5-hydroxy-2'-deoxyuridine, 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine or tetrahydrofuranyl
-
?
DNA
fragments of DNA
-
the beta-elimination reaction breaking the C3'-O-P bond 3' to an AP site can be followed by a delta-elimination reaction breaking the C5'-O-P bond 5' to the AP site, with the release of an unsaturated derivative of the base-free sugar and the generation of a gap flanked by 3'-phosphate and 5'-phosphate ends
-
?
DNA
fragments of DNA
-
recognizes urea, an oxidative ring fragmentation product of thymine
-
?
DNA
fragments of DNA
-
when DNA containing thymine glycol is used as substrate the combined N-glycosylase/AP endonuclease activity is about 2fold higher than the AP endonuclease activity
-
?
DNA
fragments of DNA
-
KsgA has al DNA glycosylase/AP lyase activity for C mispaired with oxidized T
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
specificity
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
C4'-oxidized abasic sites are efficiently excised via intermediate Schiff-base formation. Activity is 100fold less efficient than repair by exonuclease III
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
endonuclease III plays an important cellular role by removing premutagenic pyrimidine damages produced by reactive oxygen species. EcoNth is a bifunctional enzyme that has DNA glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
the enzyme forms a Schiff base-type intermediate with the substrate after the damaged base is removed
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
enzyme also has DNA N-glycosylase activity
-
-
?
additional information
?
-
-
all known bacterial AP lyases and some at least of the mammalian ones, also acts as DNA glycosylases
-
-
?
additional information
?
-
-
bacteriophage T4 endonuclease V and Escherichia coli endonuclease II catalyze N-glycosylase and 3'-abasic endonuclease reaction, beta-elimination reaction
-
-
?
additional information
?
-
-
pdT8d(-)dTn is cleaved by endonuclease III yielding two products which have the same electrophoretic behaviour as the doublet obtained by alkaline beta-elimination, thus the enzyme is a beta-elimination catalyst
-
-
?
additional information
?
-
-
KsgA does not remove C opposite normal bases, 7,8-dihydro-8-oxoguanine and 2-hydroxyadenine, KsgA does not excise thymine glycol, 5-formyluracil, and 5-hydroxymethyluracil opposite cytosine from double-stranded oligonucleotides
-
-
?
additional information
?
-
Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site)
-
-
?
additional information
?
-
-
Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site)
-
-
?
additional information
?
-
analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III using oligonucleotide duplexes containing 5,6-dihydrouracil, a natural abasic site, its tetrahydrofuran analogue, and undamaged duplexes carried fluorescent DNA base analogues 2-aminopurine and 1,3-diaza-2-oxophenoxazine as environment-sensitive reporter groups, pre-steady-state kinetic analysis, overview. Endo III induces several fast sequential conformational changes in DNA during binding, lesion recognition, and adjustment to a catalytically competent conformation. The glycosylase uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as DNA lesion sensors
-
-
?
additional information
?
-
-
analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III using oligonucleotide duplexes containing 5,6-dihydrouracil, a natural abasic site, its tetrahydrofuran analogue, and undamaged duplexes carried fluorescent DNA base analogues 2-aminopurine and 1,3-diaza-2-oxophenoxazine as environment-sensitive reporter groups, pre-steady-state kinetic analysis, overview. Endo III induces several fast sequential conformational changes in DNA during binding, lesion recognition, and adjustment to a catalytically competent conformation. The glycosylase uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as DNA lesion sensors
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA
fragments of DNA
-
-
170706, 288783, 646938, 648625, 648627, 648629, 648630, 648631, 648637, 648649, 648650, 648651, 648652, 648654, 648655, 648657, 648664, 648665, 648671, 648678, 648679
-
-
?
DNA containing apurinic/apyrimidinic sites
fragments of DNA
-
C4'-oxidized abasic sites are efficiently excised via intermediate Schiff-base formation. Activity is 100fold less efficient than repair by exonuclease III
-
-
?
additional information
?
-
Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site)
-
-
?
additional information
?
-
-
Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
KCl
Zn2+
-
Divalent metal content, Zn3-site mutations result in major activity loss, whereas Zn1 and Zn2 ligand mutations cause low to severe loss of catalytic efficiency. In the DNA-free wild-type enzyme structure, two metal ions (Zn1 and Zn2) are partially buried from solvent and bind a bridging hydroxide anion. The third metal ion (Zn3) is mostly solvent accessible, is distant from Zn1 and Zn2 and ligates a tightly bound water molecule to complete its coordination shell
additional information
-
equal or higher activity for Zn2+ or Mn2+- containing Endo IV suggests that one site may favor Mn2+ over Zn2+
Iron
-
native enzyme contains a single [4Fe-4S] cluster in the 2+ oxidation state with a net spin of zero
Iron
-
[4Fe-4S] cluster is not directly involved in catalytic mechanism and therefore has most likely a structural role
KCl
-
optimal concentration: 0.05-0.1 M, activity against apurinic and apyrimidinic sites, 50% inhibition at 0.02 and 0.12 M
KCl
-
optimal concentration: 0.10 M, activity against OsO4-sites, 50% inhibition at 0.05 and 0.15 M
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Harmane
-
i.e. 1-methyl-9H-pyrido-[3,4-b]indole, inhibits Escherichia coli endonuclease III and its associated dihydroxythymidine-DNA glycosylase activity, 50% inhibition at 0.4 mM, 80% inhibition at 1 mM
Mg2+
-
selectively inhibits endonuclease III activity when apurinic/apyrimidinic DNA is used as substrate, but has no effect when DNA containing either urea or thymine glycol is used as substrate
oligonucleotide containing 2'-fluorinated 5R- or 5S-thymidine glycol
-
inhibits DNA glycosylase activity, not the AP lyase step, in the Endo III reaction, by stabilizing the glycosidic bond
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000036 - 0.000133
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
0.0000097 - 0.004
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
0.0000059 - 0.00192
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
0.00025
DNA with 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
-
pH 7.5, 37°C
0.0000035
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite T
0.0000066
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite C
0.0000085
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite G
0.000038
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite A
0.000042
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite G
0.000054
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant deltaQLY, Nei placed opposite G
0.000077
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite G
0.00014
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite C
0.00016
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite T
0.00016
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite A
0.00026
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite A
0.00027
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite C
0.0014
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite T
0.00058
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite G
0.00061
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite A
0.00068
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite C
0.0013
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite T
0.0000023
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite G
0.0000032
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite A
0.0000044
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite C
0.0000044
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite T
0.000049
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant QLY/AAA, Nei placed opposite G
0.000066
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant deltaQLY, Nei placed opposite A
0.00019
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant QLY/AAA, Nei placed opposite T
0.00024
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant Q261A, Nei placed opposite G
0.0000023
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite G
0.0000046
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite T
0.0000047
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite C
0.000016
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite A
0.00021
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant Q261A, Nei placed opposite G
0.000000083
DNA containing apurinic/apyrimidinic sites
wild-type, Nei placed opposite A
-
0.00000011
DNA containing apurinic/apyrimidinic sites
wild-type, Nei placed opposite G
-
0.000022
DNA containing apurinic/apyrimidinic sites
mutant QLY/AAA, Nei placed opposite G
-
0.000028
DNA containing apurinic/apyrimidinic sites
mutant QLY/AAA, Nei placed opposite A
-
0.0000091
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
-
pH 7.6, 37°C, wild-type enzyme
-
0.14
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000036
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
pH 7.6, 37°C, wild-type enzyme
-
0.000133
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000097
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
pH 7.6, 37°C, wild-type enzyme
-
0.004
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000059
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
pH 7.6, 37°C, wild-type enzyme
-
0.00192
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.000088
AP-DNA
-
wild-type in rAP-containing oligonucleotide cleavage assay
-
0.00012
AP-DNA
-
mutant Y72F in rAP-containing oligonucleotide cleavage assay
-
0.0075
AP-DNA
-
mutant Y72A in rAP-containing oligonucleotide cleavage assay
-
0.011
AP-DNA
-
mutant R37A in rAP-containing oligonucleotide cleavage assay
-
additional information
AP-DNA
-
not detected in mutant E261Q in rAP-containing oligonucleotide cleavage assay
-
additional information
additional information
pre-steady-state kinetic analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III
-
additional information
additional information
-
pre-steady-state kinetic analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.098
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
0.075 - 1.6
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
0.0158
DNA containing 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
-
pH 7.5, 37°C
-
0.0000048
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant deltaQLY, Nei placed opposite G
0.000013
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite C
0.000015
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite G
0.000023
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite A
0.000065
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite G
0.000067
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite T
0.00007167
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite A
0.000583
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite A
0.003167
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite T
0.008167
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite C
0.01167
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite T
0.013
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite C
0.07167
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite G
0.00783
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite A
0.01317
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite G
0.01583
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite C
0.023
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite T
0.0025
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant deltaQLY, Nei placed opposite A
0.00583
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant Q261A, Nei placed opposite G
0.016
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant QLY/AAA, Nei placed opposite G
0.02167
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant QLY/AAA, Nei placed opposite T
0.03
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite G
0.035
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite A
0.04167
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite C
0.0483
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite T
0.00567
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant Q261A, Nei placed opposite G
0.0112
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite T
0.0115
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite C
0.023
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite A
0.0567
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite G
0.0015
DNA containing apurinic/apyrimidinic sites
mutant QLY/AAA, Nei placed opposite A
-
0.00183
DNA containing apurinic/apyrimidinic sites
mutant QLY/AAA, Nei placed opposite G
-
0.00883
DNA containing apurinic/apyrimidinic sites
wild-type, Nei placed opposite G
-
0.01067
DNA containing apurinic/apyrimidinic sites
wild-type, Nei placed opposite A
-
0.03
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
-
pH 7.6, 37°C, wild-type enzyme
-
1.37
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.043
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
pH 7.6, 37°C, wild-type enzyme
-
0.17
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.098
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
pH 7.6, 37°C, wild-type enzyme
-
0.098
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.075
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
pH 7.6, 37°C, wild-type enzyme
-
1.6
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
pH 7.6, 37°C, mutant enzyme R184A
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Activity is determined with phage T4 AP DNA endonuclease assay agrees with divalent metal (Mn2+ and Zn2+) content measured for purified His-tagged Endo IV wild-type and mutant proteins, except for E261Q and to a lesser extent E145Q, which are adjacent in the active site. Mutations of the first-shell metal-ion binding residues resulted in mild (10fold reduction activity, H109N and D179N), severe (100-2600fold reduction in activity, H69N, H182N, D229N, H216N and H231N) or complete loss (E145Q, E261Q) of catalytic activity in both the T4 AP-DNA endonuclease assay and the AP-oligonucleotide cleavage assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 8.1
-
pH 6.2 and pH 8.1: 50% of activity maximum, activity against OsO4-treated DNA
7.2 - 7.8
-
pH 7.2 and pH 7.8: 50% of activity maximal, activity against apyrimidinic and apurinic sites
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
ExoIII rapidly loses activity with preheating at more than 40°C, and almost completely lose it at 55°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
endonuclease III belongs to the DNA glycosylases of the helix-hairpin-helix-GPD structural superfamily
physiological function
Endonuclease III (Endo III) is a bifunctional DNA glycosylase possessing N-glycosylase and AP lyase activities. Endonuclease III is responsible for base excision repair of oxidized or reduced pyrimidine bases
additional information
additional information
endonuclease III uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as lesion sensors. The principal amino acids involved in the catalysis are Lys120 and Asp138. The former is the nucleophile that attacks the C1' atom of deoxyribose, resulting in the cleavage of the N-glycosydic bond and subsequent formation of a Schiff base covalent intermediate. The following beta-elimination reaction leads to the departure of the 3'-phosphate. The subsequent Schiff base hydrolysis releases the enzyme and leads to formation of a single-strand break in DNA duplex with an alpha/beta-unsaturated aldehyde at the 3'-end and a phosphate at the 5'-end
additional information
-
endonuclease III uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as lesion sensors. The principal amino acids involved in the catalysis are Lys120 and Asp138. The former is the nucleophile that attacks the C1' atom of deoxyribose, resulting in the cleavage of the N-glycosydic bond and subsequent formation of a Schiff base covalent intermediate. The following beta-elimination reaction leads to the departure of the 3'-phosphate. The subsequent Schiff base hydrolysis releases the enzyme and leads to formation of a single-strand break in DNA duplex with an alpha/beta-unsaturated aldehyde at the 3'-end and a phosphate at the 5'-end
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
-
bacteriophage T4 infected, SDS-PAGE, T4 endonuclease V (EC 3.1.25.1) possesses both pyrimidine dimer DNA glycosylase activity and apurinic/apyrimidinic DNA endonuclease EC 4.2.99.18 activity in a single polypeptide chain
33100
-
theoretical molecular weight of the hexahistidine-tagged protein, confirmed by SDS-PAGE analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
combination of dialysis and seeding techniques, sitting drop vapor diffusion method
-
Crystals are grown by vapor diffusion. The 1.10-A resolution DNA-free and the 2.45-A resolution DNA-substrate complex structures capture substrate stabilization by Arg37 and reveal a distorted Zn3-ligand arrangement that reverts, after catalysis, to an ideal geometry suitable to hold rather than release cleaved DNA product. Coordinates and structure factors for the three structures (E261Q-phosphate, E261Q-AP DNA and Y72A-AP DNA) have been deposited with accession codes 2NQH, 2NQJ and 2NQ9
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deltaQLY69-71
deletion of the entire loop, interferes with eversion of the damaged base from the helix, deficient in processing damaged DNA
Q261A
perturbs the conserved zinc finger, deficient in processing damaged DNA, can be reductively cross-linked to damaged base-containing DNA, deficient in regenerating free enzyme from the Nei-DNA covalent complex formed during the reaction
QLY69-71AAA
all amino acids in the QLY loop substituted with alanines, interferes with eversion of the damaged base from the helix, deficient in processing damaged DNA
R171A
perturbs the conserved zinc finger, deficient in processing damaged DNA
D44V
-
mutant retains glycosylase activity against oxidized pyrimidines, but the apparent rate constant for the lyase activity is significantly lower than the wild-type value
R184A
-
mutant enzyme maintains lyase activity but exhibits glycosylase specificity different from wild-type enzyme
R37A/E261Q
-
shows a three-fold decrease in AP-DNA binding affinity (Kd 340 nM)
S39L
-
mutant does not have significant glycosylase activity for oxidized pyrimidines, alhough it maintains AP lysae activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several months in 100 mM potassium phosphate, 50% glycerol pH 6.6
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap column chromatography, HiTrap heparin column chromatography, HiTrap Blue column chromatography, glutathione-Sepharose 4B column chromatography, hydroxyapatite column chromatography, and Resource S column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into vector pET-24b, recombinant plasmids maintained in Escherichia coli XL1-Blue X cells, transfected into Escherichia L21(DE3)
DNA constructs encoding mutant Endo IV enzymes are generated with the megaprimer PCR technique47 using a wild-type nfo gene sequence as template. The PCR products are purified, digested and subcloned in pET24. Hexahistidine-tagged wild-type Endo IV and mutants are subcloned in vector pET28a. The double mutants (Y72A/E261Q and R37A/E261Q) are obtained by Megaprimer mutagenesis on the E261Q mutant followed by subcloning of the PCR product in frame with an N-terminal His6-sequence in pET28a. Wild-type and mutant enzymes are produced and purified using an nfo-negative strain BW565DE3 transformed with pET24-Endo IV constructs
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
opposite-base specificity of Nei is primarily governed by residues in the Q69-Y71 loop, both Q69-Y71 loop and the zinc finger contribute significantly to the substrate specificity of Nei
additional information
-
opposite-base specificity of Nei is primarily governed by residues in the Q69-Y71 loop, both Q69-Y71 loop and the zinc finger contribute significantly to the substrate specificity of Nei
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakabeppu, Y.; Sekiguchi, M.
Physical association of pyrimidine dimer DNA glycosylase and apurinic/apyrimidinic DNA endonuclease essential for repair of ultraviolet-damaged DNA
Proc. Natl. Acad. Sci. USA
78
2742-2746
1981
Tequatrovirus T4, Escherichia coli
Kim, J.; Linn, S.
The mechanism of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites
Nucleic Acids Res.
16
1135-1141
1988
Tequatrovirus T4, Escherichia coli
Hatahet, Z.; Kow, Y.W.; Purmal, A.A.; Cunningham, R.P.; Wallace, S.S.
New substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase
J. Biol. Chem.
269
18814-18820
1994
Escherichia coli
Takeshita, M.; Chang, C.N.; Johnson, F.; Will, S.; Grollman, A.P.
Oligodeoxynucleotides containing synthetic abasic sites. Model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases
J. Biol. Chem.
262
10171-10179
1982
Escherichia coli
Bailly, V.; Verly, W.G.
Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst
Biochem. J.
242
565-572
1987
Escherichia coli
Manoharan, M.; Mazumder, A.; Ranson, S.C.; Gerlt, J.A.; Bolton, P.H.
Mechanism of UV endonuclease V cleavage of abasic sites in DNA determined by 13C labeling
J. Am. Chem. Soc.
110
2690-2691
1988
Tequatrovirus T4, Escherichia coli
-
Bailly, V.; Verly, W.G.
AP endonuleases an AP lyases
Nucleic Acids Res.
17
3617-3618
1989
Escherichia coli
Gossard, F.; Verly, W.G.
Properties of the main endonucleases specific for apurinic sites of Escherichia coli (endonuclease VI)
Eur. J. Biochem.
82
321-332
1978
Escherichia coli
Katcher, H.L.; Wallace, S.S.
Characterization of Escherichia coli x-ray endonuclease, endonulease II
Biochemistry
22
4071-4081
1983
Escherichia coli
Kow, Y.W.; Wallace, S.S.
Mechanismm of action of Escherichia coli endonuclease III
Biochemistry
26
8200-8206
1987
Escherichia coli
Asahara, H.; Wistort, P.M.; Bank, J.F.; Bakerian, R.H.; Cunningham, R.P.
Purification and characterization of Escherichia coli endonuclease III from the cloned m gene
Biochemistry
28
4444-4449
1989
Escherichia coli
Cunningham, R.P.; Asahara, H.; Bank, J.F.; Scholes, C.P.; Salerno, J.C.; Surerus, K.; Mnck, E.; McCracken, J.; Peisach, J.; Emptage, M.H.
Endonuclease is an iron-sulfur protein
Biochemistry
28
4450-4455
1989
Escherichia coli
Dizdaroglu, M.; Laval, J.; Boiteux, S.
Substrate specificity of the Escherichia coli endonuclease III: Excision of thymine- and cytosine-derived lesions in DNA produced by radiation-generated free radicals
Biochemistry
32
12105-12111
1993
Escherichia coli
Fu, W.; O'Handley, S.; Cunningham, R.P.; Johnson, M.K.
The role of the iron-sulfur cluster in Escherichia cloli endonuclease III. A resonance Raman strudy
J. Biol. Chem.
267
16135-16137
1992
Escherichia coli
Kuo, C.F.; McRee, D.E.; Cunningham, R.P.; Tainer, J.A.
Crystallization and crystallographic characterization of the iron-sulfur-containing DNA-repair enzyme endonuclease III form Escherichia coli
J. Mol. Biol.
227
347-351
1992
Escherichia coli
Warner, H.R.; Persson, M.L.; Bensen, R.J.; Mosbaugh, D.W.; Linn, S.
Selective inhibition by harmane of apurinic/apyrimidinic endonuclease activity of phage T4-induced UV endonuclease
Nucleic Acids Res.
9
6083-6092
1981
Tequatrovirus T4, Escherichia coli, Homo sapiens
Chaudhry, M.A.; Weinfeld, M.
Reactivity of human apurinic/apyrimidinic endonuclease and Escherichia coli exonuclease III with bistranded abasic sites in DNA
J. Biol. Chem.
272
15650-15655
1997
Escherichia coli, Homo sapiens
Chaudhry, M.A.; Weinfeld, M.
The action of Escherichia coli endonuclease III on multiply damaged sites in DNA
J. Mol. Biol.
249
914-922
1995
Escherichia coli
Ishchenko, A.A.; Sanz, G.; Privezentzev, C.V.; Maksimenko, A.V.; Saparbaev, M.
Characterisation of new substrate specificities of Escherichia coli and Saccharomyces cerevisiae AP endonucleases
Nucleic Acids Res.
31
6344-6353
2003
Saccharomyces cerevisiae, Escherichia coli
Pope, M.A.; Porello, S.L.; David, S.S.
Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates
J. Biol. Chem.
277
22605-22615
2002
Escherichia coli, Homo sapiens
Purmal, A.A.; Rabow, L.E.; Lampman, G.W.; Cunningham, R.P.; Kow, Y.W.
A common mechanism of action for the N-glycosylase activity of DNA N-glycosylase/AP lyases from E. coli and T4
Mutat. Res.
364
193-207
1996
Tequatrovirus T4, Escherichia coli
Greenberg, M.M.; Weledji, Y.N.; Kim, J.; Bales, B.C.
Repair of oxidized abasic sites by exonuclease III, endonuclease IV, and endonuclease III
Biochemistry
43
8178-8183
2004
Escherichia coli
Katafuchi, A.; Nakano, T.; Masaoka, A.; Terato, H.; Iwai, S.; Hanaoka, F.; Ide, H.
Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions
J. Biol. Chem.
279
14464-14471
2004
Escherichia coli
Watanabe, T.; Blaisdell, J.O.; Wallace, S.S.; Bond, J.P.
Engineering functional changes in Escherichia coli endonuclease III based on phylogenetic and structural analyses
J. Biol. Chem.
280
34378-34384
2005
Escherichia coli
Doi, Y.; Katafuchi, A.; Fujiwara, Y.; Hitomi, K.; Tainer, J.A.; Ide, H.; Iwai, S.
Synthesis and characterization of oligonucleotides containing 2'-fluorinated thymidine glycol as inhibitors of the endonuclease III reaction
Nucleic Acids Res.
34
1540-1551
2006
Escherichia coli
Kropachev, K.Y.; Zharkov, D.O.; Grollman, A.P.
Catalytic mechanism of Escherichia coli endonuclease VIII: roles of the intercalation loop and the zinc finger
Biochemistry
45
12039-12049
2006
Escherichia coli (P50465), Escherichia coli
Kaneda, K.; Ohishi, K.; Sekiguchi, J.; Shida, T.
Characterization of the AP endonucleases from Thermoplasma volcanium and Lactobacillus plantarum: Contributions of two important tryptophan residues to AP site recognition
Biosci. Biotechnol. Biochem.
70
2213-2221
2006
Escherichia coli, Lactiplantibacillus plantarum, Thermoplasma volcanium
Garcin, E.D.; Hosfield, D.J.; Desai, S.A.; Haas, B.J.; Bjoeras, M.; Cunningham, R.P.; Tainer, J.A.
DNA apurinic-apyrimidinic site binding and excision by endonuclease IV
Nat. Struct. Mol. Biol.
15
515-522
2008
Escherichia coli, Escherichia coli BW565DE3
Zhang-Akiyama, Q.M.; Morinaga, H.; Kikuchi, M.; Yonekura, S.; Sugiyama, H.; Yamamoto, K.; Yonei, S.
KsgA, a 16S rRNA adenine methyltransferase, has a novel DNA glycosylase/AP lyase activity to prevent mutations in Escherichia coli
Nucleic Acids Res.
37
2116-2125
2009
Escherichia coli, Escherichia coli KSR7
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